Functional Protein Derived From Animal Muscle Tissue or Mechanically Deboned Meat and Method For Making The Same

ABSTRACT

A process for producing a protein product for addition to raw meat wherein the source of the protein product is animal muscle or mechanically deboned meat. The animal muscle tissue is homogenized. Protein in the homogenate is solubilized. Solubilized homogenate is heated to a temperature required for pasteurization and/or sterilization according to known standards. The homogenate is then optionally adjusted to a value at which the protein precipitates. The protein product of the present invention is free of bacteria and toxins and can be used as meat or added to raw meat for delivery to a consumer as uncooked meat.

RELATED APPLICATIONS

This application is a continuation of U.S. application Ser. No.16/148,720, entitled, “Functional Protein Derived From Animal MuscleTissue or Mechanically Deboned Meat and Method for Making the Same byStephen D. Kelleher et al., filed Oct. 1, 2018, which claims the benefitof U.S. Provisional Application No. 62/567,041, entitled, “FunctionalProtein Derived From Animal Muscle Tissue or Mechanically Deboned Meatand Method For Making The Same” by Stephen D. Kelleher, et al., filedOct. 2, 2017 and application Ser. No. 16/148,720 is acontinuation-in-part of U.S. application Ser. No. 14/506,615, entitled,“Functional Protein Derived From Animal Muscle Tissue or MechanicallyDeboned Meat and Method for Making the Same” by Stephen D. Kelleher, etal., filed Oct. 4, 2014, which claims the benefit of U.S. ProvisionalApplication No. 61/886,889, filed Oct. 4, 2013, entitled, “ProteinDerived From Animal Muscle Tissue Or Mechanically Deboned Meat AndMethod For Making The Same Using Food Preservation Methods” by StephenD. Kelleher, et al.

The entire teachings of the above applications are incorporated hereinby reference.

BACKGROUND OF THE INVENTION

Over a number of years research has been directed to the isolation ofproteins from animal muscle tissue and the application of such isolatedproteins to various foods to achieve improved functionality incomparison with foods cooked without such proteins. For example, whencertain of these prior art proteins have been sprayed onto food to becooked by frying, the cooked food has a reduced fat content over foodthat does not include such protein. In other applications, food cookedwith the addition of such prior art protein, as by injection, retainsmore moisture than untreated cooked food.

Food safety is an important concern in today's modern food processingplants and methods are often being sought after to reduce overallbacteria or pathogen counts. For some foods, pasteurization is selectedas a food preservation method; in others, sterilization. In manycountries, such as Australia, the importation of meat products into acountry requires that the meat products be either pasteurized orsterilized before such products can be imported to that country.

When harvesting has been completed, some animal muscle tissue remainsattached to bones. Such attached animal muscle tissue is a potentiallycommercially viable animal muscle tissue for obtaining protein.“Deboning” is a process for recovering such residual animal muscletissue from the bones. During deboning animal muscle tissue is separatedfrom a bone by scraping, shaving or pressing the attached animal muscletissue from the bone. Deboned product is called “deboned meat” or“separated meat.” While such a process theoretically could provide aneconomical source of animal muscle tissue for the isolation of protein,commercial deboning commonly tests high in bacteria and/or positive infood-borne pathogens, including salmonella. Due to the inherent risk ofthese bacteria many food processors require any product includingmechanically deboned meat or even protein obtained from mechanicallydeboned meat be fully cooked for human consumption for health reasonsand not sold in a raw state. Specifically, a food processing companymust heat a “ready-to-eat” product to an internal temperature of atleast 160° F. to achieve a lethality in the range of 6.5-log₁₀ to7.0-log₁₀. This requirement limits the applications for mechanicallydeboned meat primarily by imposing significant manufacturing costs andby producing a meat product that is “well done” and that loses moistureduring cooking.

A need exists for a procedure that could assure pasteurization orsterilization of meat products without reducing the meat'sfunctionality. Also, a further need exists for a procedure that couldutilize a starting material that is potentially inherently high inpathogens, such as deboned meat. Yet, a further need exists for a foodpreparation method for obtaining protein from animal meat ormechanically deboned meat whereby the protein product can be consumedalone or added to raw meat such that the final product meets or exceedsthe government and commercial standards for bacteria and toxic contentwithout cooking the raw meat and that retains moisture prior to aconsumer's cooking the final product.

SUMMARY OF THE INVENTION

This invention generally relates to protein compositions derived fromanimal muscle tissue for incorporation into raw food and morespecifically provides a protein composition with a reduced risk of beingcontaminated by various microorganisms.

Therefore, it is an object of this invention to provide a process bywhich a protein product can be obtained from animal muscle ormechanically deboned meat that can be consumed alone or added to meat sothat a final product meets or exceeds government and commercialregulations and a corresponding protein product.

Another object of this invention is to provide a process by which aprotein product obtained from animal muscle tissue or deboned (e.g.,mechanically deboned) meat can be added to raw meat to obtain a finalproduct without cooking the final product and corresponding proteinproduct.

Still another object of this invention is to provide a protein productobtained from animal muscle tissue or mechanically deboned meat that canbe added to raw meat without cooking while retaining the functionalityof the raw meat.

In accordance with one aspect this invention a process for producing apasteurized or sterilized protein product from animal muscle tissueobtained from raw meat or mechanically deboned meat for application toraw meat includes homogenizing the animal muscle tissue from the rawmeat or mechanically deboned animal muscle tissue (optionally in water).After adjusting the pH of the homogenate to solubilize the protein, theprocess elevates temperature of the homogenate to an internaltemperature required for pasteurization or sterilization for at least arequired time. The homogenate is then optionally chilled to anintermediate temperature whereupon the protein is optionallyprecipitated from the homogenate. The moisture content can then beadjusted to a desired value. As the protein product has been pasteurizedor sterilized, there is no need for cooking a meat product containingthe protein product, and such a protein product would meet or exceedbacterial standards established by an importing country.

In accordance with another aspect of this invention, a process forproducing a pasteurized or sterilized protein product from animal muscletissue obtained from animal meat for application to raw meat is obtainedby mixing and homogenizing the animal muscle tissue and water. In anembodiment, homogenizing the animal muscle tissue can be done withoutthe addition of water. After adjusting the pH of the homogenate tosolubilize the protein, the process elevates the temperature of the pHadjusted homogenate to an internal temperature required forpasteurization or sterilization. The homogenate is then optionallychilled to an intermediate temperature. Depending on the protein productuse, in some embodiments, the protein can be precipitated from thechilled homogenate by adjusting the pH of the homogenate into theisoelectric range. Then the process dewaters the protein to a desiredmoisture content.

The present invention includes protein produce and a method or processfor producing a protein product wherein the protein product has areduced pathogen level, retains a functionality of raw meat and has acolor in range between about 75 to 20 L* about 32 to 4 a*, and about 23to 3 b*. The steps of the method include homogenizing the animal muscletissue, optionally in water, to thereby obtain a homogenate andadjusting the pH of the homogenate to solubilize the protein to obtain asolubilized liquid protein solution. The pH adjustment for solubilizingthe protein includes the addition of a food grade base to obtain a pHvalue in the range between about 8.3 and about 10.5, or in anotherembodiment includes addition of a food grade acid to obtain a pH valuein the range between about 3.6 and about 4.2. The solubilized liquidprotein solution is then pasteurized or sterilized. Specifically, thisstep includes elevating the temperature of the solubilized liquidprotein solution to an internal temperature of 158° F. or above for atleast an instant, or to an internal temperature of about 130° F. andabout 157° F. for at least between about 14 seconds to about 121 minutessuch that the solubilized liquid protein solution is pasteurized,sterilized or both to obtain a solubilized liquid protein solution witha reduced pathogen level (e.g., wherein the reduced pathogen levelcomprises at least a reduction in salmonella by 6.5 log₁₀). The methodof the present invention further involves optionally chilling thesolubilized liquid protein solution with the reduced pathogen level toan intermediate temperature to obtain a chilled liquid protein solution.In an embodiment, the liquid protein solution is precipitated to therebyobtain a precipitated protein. The method/process results in aprecipitated protein has reduced pathogen level as compared to aprecipitated protein that has not undergone the steps of the presentinvention. The precipitated protein also retains the functionality ofraw meat and has “red” color in range between about 75 to 20 L*, about32 to 4 a*, and about 23 to 3 b*.

In an aspect, precipitating the protein from the chilled liquid proteinsolution includes the adding a food grade acid or base to obtain a pH ator near the isoelectric point, or a pH to a value in the range of4.2≤pH≤6.4. In another aspect, precipitating the protein from thechilled liquid protein solution encompasses adding salt. Food grade baseused in either the solubilization step or precipitation step, forexample, includes solution sodium bicarbonate, sodium carbonate,potassium bicarbonate, potassium carbonate, sodium hydroxide anycombination thereof. Similarly, food grade acid used in either thesolubilization step or precipitation step encompasses, e.g., citricacid, phosphoric acid, ascorbic acid, hydrochloric acid and anycombination thereof.

The method of the present invention can further include, in anembodiment, the step of assessing the functionality of the precipitatedprotein. Protein having a “red” color, as described herein, is acharacteristic of raw meat and is considered to be functional.Functionality can be measured using a water binding test, meat emulsiontest, moisture retention test, a color test (e.g., can be observed orcolor values can be measured) and a combination thereof. The process ofthe present invention can further include dewatering the precipitate, inan embodiment, to a desired moisture content.

As described above, the present invention includes a protein product andmethods with the steps described herein, but the precipitation step, inone embodiment, is optional. In the case in which the precipitation stepis not preformed, the solubilized liquid protein solution is the proteinproduct, as is, or modified as desired. In such an embodiment, addingthe solubilized liquid protein solution with the reduced pathogen levelto the animal muscle tissue refers to injecting the solubilized liquidprotein solution with the reduced pathogen level into the animal muscletissue. Alternatively, the solubilized liquid protein solution with thereduced pathogen level can be sprayed or applied onto one or moresurfaces of the animal muscle tissue. In other embodiments, thesolubilized liquid protein solution can be dewatered to a desiredmoisture content or spray-dried.

BRIEF DESCRIPTION OF THE DRAWINGS

The appended claims particularly point out and distinctly claim thesubject matter of this invention. The various objects, advantages andnovel features of this invention will be more fully apparent from areading of the following detailed description in conjunction with theaccompanying drawing.

FIG. 1, is a flow chart that describes one embodiment of a process thatutilizes a pasteurized/sterilized protein precipitate.

FIG. 2, is a flow chart that describes one embodiment of a process thatutilizes a pasteurized/sterilized solubilized liquid protein solution.

DETAILED DESCRIPTION OF THE INVENTION

A pasteurizing or sterilizing process 10 or 110 for a protein productderived from raw meat or mechanically deboned meat is shown in thefigures. Process 10 or 110, shown in FIGS. 1 and 2, respectively,enables animal muscle tissue or deboned meat to serve as a proteinsource for application to raw meat so that the final product meets orexceeds standards for various bacteria and toxic contents without theneed for cooking. That is, such protein can be used “as is” (e.g., ashamburger, hotdog stuffing, or sausage stuffing), added to uncooked meat(such as poultry), as a marinade, or spray dried as a protein powder,thereby enabling the sale of the pasteurized/sterilized protein forhuman consumption. The pasteurization step eliminates bacterialpathogens of concern for meat products such as salmonella in poultry,and sterilization produces a final product with the added security ofeliminating bacterial spores as well as vegetative pathogenic bacteria.Consequently, if a food processor in a country can supply raw meataccording to the government and commercial regulations of that country,the food processor can import the pasteurized or sterilized proteinproduct without a concern that the combination of the raw meat and theprotein product will affect the quality of the mixed meat and proteinproduct.

As shown in the FIGS. 1 and 2, food pasteurization/sterilization process10 or 110 uses step 12 or 112 to mix the animal muscle (meat) ormechanically deboned meat and chilled water. The types of meat that canbe used in the steps of the present invention include beef, poultry,fish or other muscle tissue from an animal. Step 12 or Step 112 involvesmixing mechanically deboned meat with water in a ratio of parts of meatto water ranging from about 1:9 to about 1:3. The water can optionallybe added immediately after deboning, or sometime after deboning themeat, or during homogenization. The temperature of the chilled waterranges from just above the freezing point to a point below roomtemperature. For example, the temperature of the chilled water rangesfrom about 34° F. to about 45° F. (e.g., 34, 35, 36, 37, 38, 39, 40, 41,42, 43, 44, 45° F.), and in an embodiment is between 37° F. and about40° F. When performed, Step 12 or Step 112 results in a chilled mixtureof water and deboned meat. Alternatively, Step 12 or Step 112 can usecool tap water, and adding water is optional.

In Step 14 or Step 114, this chilled mixture is then homogenized.Homogenization refers to a process in which the particles in a mixturebecome uniform or evenly distributed. In the case of the presentinvention, Step 14 or Step 114 homogenizes the deboned meat and chilledwater (optional) so that the meat is uniformly present throughout theliquid solution (i.e., a “homogenate”). In an embodiment, adding wateris optional and when not added during mixing or homogenization, it needonly be added to dilute the acid or base. Homogenization can occur usingany commercially available apparatus such as a food chopper orcutting/dispersion machine. Examples of such machines that can be usedhomogenize the chilled mixture include STEPHAN MICROCUT cutting anddispersing systems (Hamelin, Germany), KARL SCHNELL mixers (New London,Wis.) or WARING Model WSB immersion blenders. The length of time neededto achieve a uniform homogenate depends on the amount of the chilledmixture, the type of motor on the apparatus, and capacity of the machinebeing used. In an embodiment, homogenization can be performed in a timeranging between about 30 seconds and about 15 minutes (e.g., between 40seconds and about 2 minutes) and typically the average particle size inthe homogenate ranges between about 100 μM (microns) and about 1millimeter preferably between about 150 μM (microns). In an aspect, theaddition of chilled water to the deboned meat, and homogenizing canhappen simultaneously or there can be overlap between the steps (e.g., aportion of the chilled water can be added gradually after chopper hasbeen turned on). During the homogenization step, it is believed that theavailable surface area of the protein is increased so that it canbetter, more effectively solubilize in the next step, Step 16 or Step116.

In Step 16 or Step 116, the protein homogenate from Step 14 or Step 114is solubilized. Solubility can occur with the addition of a food gradeacid or base. As used herein, “solubilized protein” refers to theprotein being dissolved in liquid or put into solution. In anembodiment, acid or base is added in a sufficient amount andconcentration to allow the protein to dissolve or solubilize withoutdenaturing the protein. Any food grade acid or base can be used toadjust the pH to ranges described herein to solubilize the protein.Examples of such bases include sodium bicarbonate, sodium carbonate,potassium bicarbonate, potassium carbonate, or sodium hydroxide.Similarly, examples of food grade acids that can be used for the presentinvention include citric acid, phosphoric acid, ascorbic acid orhydrochloric acid. Other acids or bases, previously known or laterdeveloped, can be used in the steps of the present invention so long asthey solubilize (and/or precipitate, as the case may be) the proteinunder conditions described herein and are food grade or biocompatible.The volume and concentration of the acid or base used to solubilize theprotein at the desired pH will depend on the starting pH of thesolution, and the volume of the solution being brought to the proper pH.The concentration of the food grade acid or base will depend on theparticular acid or base being used and the composition (e.g., liquid orpowder forms) but ranges between about 0.5M to about 3M (e.g., betweenabout 1M and about 2 M) (molarity) or between 0.2% to about 90% w/w %(approximate strength). In an embodiment, sodium carbonate can be usedin a concentration between about 0.7% and about 10% solution, and sodiumbicarbonate can be used in a concentration between about 0.5% to about10% solution (e.g., between about 5 and 6%) with water. Additionally,when using sodium bicarbonate it can be used as a powder added directlyto the protein. In the case of citric acid, a concentration of about 2M(e.g., between about 0.5M and about 3M) and in the case of hydrochloricacid, a concentration of 1M (e.g., between 0.2 and about 2M) can be usedto solubilize the protein. With respect to phosphoric acid, an 85%strength can be used. In the case of citric acid and phosphoric, about0.3% and about 1% by weight can be used, and for hydrochloric acid, arange of about 0.2 to about 0.5% by weight can be used with the steps ofthe present invention. When using ascorbic acid with the methods of thepresent invention, its powder/crystalline form can be used in which casethe ascorbic acid power can be added directly to the homogenate. Thechoice of the food grade acid and its concentration should be one thatdoes not denature the protein in the homogenate. In an embodiment, tosolubilize the protein, the base adjusts the pH of the homogenate toobtain a resulting pH in the range of equal to or between about 8.3 andabout 10.5 (e.g., about 8.4, 8.5, 8.6, 8.7, 8.9, 9.0, 9.1, 9.2, 9.3,9.4, 9.5, 9.6, 9.7, 9.8, 9.9, 10.0, 10.1, 10.2, 10.3, 10.4). When usingacid to solubilize the protein, the food grade acid adjusts the pH ofthe homogenate to obtain a resulting pH in the range of equal to orbetween about 3.6 and about 4.2 (e.g., about 3.6, 3.7, 3.8, 3.9, 4.0,4.1 and 4.2). In an embodiment, solubilization of the homogenate refersto the protein being mostly solubilized or in solution. In anotherembodiment, solubilization refers to the solution having least about 75%(e.g., 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100%) of the proteinsolubilized. Once the protein is solubilized, it is referred to as a“solubilized liquid protein solution.” One can proceed to the next step,Step 18 or Step 118.

Step 18 or Step 118 heats the adjusted pH homogenate with thesolubilized liquid protein solution to an internal temperature for aspecified time that meets or exceeds government and commercialregulations that define the temperature and time required forpasteurization or sterilization. For example, the charts below are thecurrent governmental guidelines to pasteurize beef, poultry or fish.Obtaining meat that is safe for human consumption using thepasteurization process is a function of the type of meat, thetemperature and the desired lethality/reduction in salmonella.Generally, salmonella is one of the more difficult bacteria to reduce tosafe levels and is used as benchmark for determining the safety of humanconsumption of meat. Often, if the pasteurization/sterilization step isable to reduce salmonella by at least about 6.5 (e.g., or about 7) on alog 10 scale, then other harmful bacteria are also considered to bereduced (excluding harmful spores which are reduced by sterilization).

TABLE 1 FSIS, Appendix A for Beef Minimum Internal Minimum processingtime in minutes or seconds Temperature after minimum temperature isreached Degrees Degrees 6.5-Log10 7-Log10 Fahrenheit CentigradeLethality Lethality 130 54.4 112 min. 121 min. 131 55.0 89 min. 97 min.132 55.6 71 min. 77 min. 133 56.1 56 min. 62 min. 134 56.7 45 min. 47min. 135 57.2 36 min. 37 min. 136 57.8 28 min 32 min. 137 58.4 23 min.24 min. 138 58.9 18 min 19 min. 139 59.5 15 min. 15 min. 140 60.0 12min. 12 min. 141 60.6 9 min 10 min. 142 61.1 8 min. 8 min. 143 61.7 6min 6 min 144 62.2 5 min. 5 min. 145 62.8 4 min.* 4 min.* 146 63.3 169sec. 182 sec. 147 63.9 134 sec 144 sec. 148 64.4 107 sec 115 sec. 14965.0 85 sec 91 sec. 150 65.6 67 sec. 72 sec. 151 66.1 54 sec 58 sec. 15266.7 43 sec. 46 sec. 153 67.2 34 sec 37 sec 154 67.8 27 sec. 29 sec 15568.3 22 sec. 23 sec. 156 68.9 17 sec. 19 sec. 157 69.4 14 sec. 15 sec.158 70.0 0 sec.** 0 sec.** 159 70.6 0 sec.** 0 sec.** 160 71.1 0 sec.**0 sec.** *Past regulations have listed the minimum processing time forroast beef cooked to 145° F. as “Instantly.” However, due to their largesize, most of these roasts dwell at 145° F., or even at highertemperatures, for at least 4 minutes after the minimum internaltemperature is reached. FSIS has revised this time/temperature table toreflect this and emphasizes that, to better ensure compliance with theperformance standard, establishments should ensure a dwell time of atleast 4 minutes if 145° F. is the minimum internal temperature employed.**The required lethalities are achieved instantly when the internaltemperature of a cooked meat product reaches 158° F. or above.

As can be seen in Table 1, the pasteurization temperature ranges fromabout 130° F. to about 160° F., and the time ranges from about 0 or 0.1seconds (instantaneous) to about 121 minutes such that 6.5 log 10 (e.g.,or about 7 log 10) salmonella bacteria is reduced to acceptable levels.In an embodiment, pasteurization can be achieved merely by heating afood product until the internal temperature is elevated to at least 158°F. (72° C.) for at least an instant. Once this internal temperature of158° F. is reached, then the bacteria die with minimal time (i.e., 0 or0.1 seconds). Put another way, the Table 1 shows that in the internaltemperature range between 158° F. and about 160° F., or greater, theminimal amount of time is instantaneous. For an internal temperaturerange between about 130° F. and about 157° F., the amount of time toachieve lethality is between about 14 seconds to about 121 minutes(e.g., about 14, 20, 25, 30, 35, 40, 45, 50, 55 seconds, 1, 5, 10, 15,20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100,105, 110, 115, 120, 121 minutes) (e.g., to achieve 6.5-log¹⁰ lethalityis between about 14 seconds to about 112 minutes, and to achieve 7-log¹⁰lethality is between about 15 seconds to about 121 minutes). In anaspect, Table 1 indicates that these temperature and times are used forbeef, however, in the food industry, these temperatures and times areused for other meat types described herein. Generally, if salmonella isat safe levels when cooking beef, then it is at safe levels cookingother types of meat because this beef table is the higher of thesestandards. According to one sterilization standard, a food product mustbe heated to at least 250° F. (121° C.) and held at that temperature for10 minutes. Step 18 or Step 118 results in a composition referred toherein as a “heated homogenate,” “pasteurized/sterilized homogenate,”“solubilized liquid protein solution with the reduced pathogen levels”or “pasteurized/sterilized solubilized liquid protein.” In the case ofFIG. 2, if desired, the protein product at this point in the process isa pasteurized/sterilized marinade or injectable protein product.

The heated homogenate can then be optionally processed to separate theprotein from the lipids/fat in decision box 18A or box 118A. A two-wayseparation or three-way separation can be performed. Separation can beperformed using a disc centrifuge, a decanter centrifuge, or byfiltration. Referring to the figures, if desired, lipid separation canbe performed by using centrifugation (Step 18B or Step 118B). Ifperformed, centrifugation occurs, in an aspect, in a range between about3200 RPMs and about 5000 RPMs for between about 1 minute and about 10minutes (e.g., between about 2 and about 5 minutes) or during acontinuous operation in which the heated homogenate is continuouslyflowing throughout the system including the centrifugation. Duringcentrifugation, heated homogenate is separated to form a protein richaqueous phase and a lipid phase (e.g., a two-way separation) or aprotein rich aqueous phase, liquid fat and water are separated in onestep (e.g., a three-way separation). The lipid phase and/or water areremoved to leave a pasteurized/sterilized protein rich solution.Centrifuges that can be used for Step 18B or Step 118B include disccentrifuges from Alfa Laval (Lund, Sweden) or GEA/Westfalia, (Oelde,Germany). In the case of FIG. 2, if desired, the protein product at thispoint in the process is a reduced fat pasteurized/sterilized marinade orinjectable protein product.

After Step 18 or Step 118 raises the temperature to the pasteurizationor sterilization temperature for the specified time, if any, Step 20 orStep 120 chills the pasteurized/sterilized homogenate (e.g., solubilizedliquid protein solution with the reduced pathogen levels) to anintermediate temperature. The temperature of the pasteurized/sterilizedhomogenate is lowered to a range between the freezing point and roomtemperature. In an embodiment, the temperature at Step 20 or Step 120 islowered to a range equal to or between about 34° F. and about 45° F.(34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, or 45° F.) (equal to orbetween about 1° C. and about 4° C. (1, 2, 3, 4° C.). In an aspect, thetime to lower the pasteurized/sterilized homogenate will vary dependingon apparatus used, the volume and density of the pasteurized/sterilizedhomogenate. Once the temperature of the pasteurized/sterilizedhomogenate is uniformly lowered to the desired range, a chilled,pasteurized/sterilized homogenate is obtained and ready for the nextstep or can be used as a pasteurized/sterilized marinade or injectableprotein product.

Step 20 or Step 120 of chilling the pasteurized/sterilized homogenate isoptional. In an embodiment, the pasteurized/sterilized homogenate doesnot need to be chilled and can move directly to the next step. Thepasteurized/sterilized homogenate can be processed directly from beingpasteurized/sterilized without chilling. In certain cases, depending onthe equipment being used, the pasteurized/sterilized homogenate can coolnaturally as it is further processed. Surprisingly, even when thepasteurized/sterilized homogenate is not chilled, it continues tomaintain its “red” color, as defined herein, and other functionalcharacteristics. In other words, protein that is undergoes the steps ofthe present invention, in one aspect, can still maintain its functionalcharacteristics including “red” color even though it is heated at hightemperatures sufficient for pasteurization and/or sterilization andcontinues to be subjected to relatively high temperatures for longerperiods of time.

Devices for heating and/or chilling are known in the art andcommercially available. Step 18 or Step 118, thepasteurization/sterilization step, can be carried out by any device thatcan deliver the amount of heat needed to achieve conditions forpasteurization and/or sterilization described herein. Examples of suchdevices include heat exchangers, including falling film heat exchangersand tubular heat exchangers. Heat exchangers are able to deliver heat aswell as cool the meat and if used in present invention, can be used inSteps 18 and 20, or Steps 118 or 120. In an embodiment in which a heatexchanger is not used, a heater/oven or other device can be used toirradiate heat to accomplish step 18, and a refrigerator or othersimilar device can be used to cool the homogenate. An example of aheater is Commercial Cooking Appliance Model KR-S2 hot plate.

In the embodiment shown in FIG. 1, once the solubilized liquid proteinsolution (e.g., the solubilized liquid protein solution with the reducedpathogen levels) is obtained, the protein can be precipitated from thesolution to form a suspension of precipitated protein. In an embodiment,precipitation occurs at step 22 by adjusting the pH of the solubilizedliquid protein solution into the isoelectric range of the meat involved.The isoelectric range for meat, in general, is a pH between about 4.2and about 6.4 (e.g., a pH of about 4.2, 4.3, 4.4, 4.5, 4.6, 4.7, 4.8,4.9, 5, 0, 5.1, 5.2, 5.3, 5.4, 5.5, 5.6, 5.7, 5.8, 5.9, 6.0, 6.1, 6.2,6.3, and 6.4). The isoelectric range can depend, for instance, onconditions such as salt, the type of protein, the charge of the protein,the amino acids that make up the protein, and the ionic strength of thesolution to which the protein has been subjected. Adjusting the pH tothe aforementioned isoelectric range can be performed by adding eitheran acidic solution or a basic solution to the chilled,pasteurized/sterilized homogenate. If an acid was added in step 16 tosolubilize the protein, then base can be added in this step 22 toprecipitate the protein. Similarly, if base was added in step 16 tosolubilize the protein, then acid can be added in this step 22 toprecipitate the protein. Any food grade acid or base can be used toadjust the pH to these ranges, and examples and amounts of such acidsand bases are provided herein in the discussion of step 16. The volumeand concentration of the acid or base used to buffer the chilled,pasteurized/sterilized homogenate to the desired pH will depend on thestarting pH of the solution, and the volume of the solution beingbrought to the proper pH. In another embodiment, precipitation refers tothe suspension having least about 75% (e.g., 80%, 85%, 90%, 95%, 96%,97%, 98%, 99%, or 100%) of the protein precipitated.

In an embodiment, the precipitation step, step 22, is optional. This canbe seen in FIG. 2 in which there is no precipitation step. Thepasteurized/sterilized homogenate can be used to in its liquid solubleform as a pasteurized/sterilized injectable, for use as apasteurized/sterilized coating or spray onto animal muscle tissue, as apasteurized/sterilized marinade to form a protein product, or vacuumtumbled with a meat to form a pasteurized/sterilized marinated meatproduct or spray dried to form a pasteurized/sterilized protein powder.The pasteurized/sterilized homogenate which is still in its soluble formhas either a high pH (e.g., about 8.3 to about 10.5 (about 9.0, 9.3,9.5, 9.7, 10.0, 10.3, 10.5)) or low pH (e.g., about 3.6 and about 4.2(e.g., about 3.6, 3.7, 3.8, 3.9, 4.0, 4.1 and 4.2)), which, when coatedor sprayed onto the surface of animal muscle tissue can help to reducebacteria on the animal protein surface.

Another way to precipitate the protein from the pasteurized/sterilizedhomogenate is to add salt. Examples of salts that can be used toprecipitate the protein from solution include sodium chloride (NaCl) andpotassium chloride KCl). The concentration of NaCl or KCl ranges betweenabout 3.5% and about 8% by weight.

Referring to FIG. 1, Step 22 results in a mixture having a proteinprecipitate that has been pasteurized/sterilized (hereinafter referredto as “protein precipitate mixture” or “precipitated protein”).

The next steps performed depend on the end product (e.g., proteinproduct) desired. The end meat product can be a ground (e.g.,hamburger/sausage/hotdog) type end product, a protein marinade,injectable, spray or coating, or a protein powder.

For example, in FIG. 1, if vacuum tumbling is not required for aparticular end product, such as a marinade, decision box 22A transferscontrol to step 24 to optionally dewater the protein precipitate. Inthis step water is removed from the protein precipitate mixture by usinga strainer, decanting centrifuge or filtration. The amount of waterremoved can vary, again based on the desired end product. Step 24 thende-waters the precipitate to the desired moisture content. In oneembodiment, the moisture content of the protein precipitate mixtureafter dewatering can range from between about 90% and 99%. The resultingprotein is one that is of a hamburger/sausage stuffing texture (alsoreferred to as “dewatered precipitate”).

If a protein powder is desired, one can decide to spray dry thedewatered precipitate or solubilized liquid protein solution, causingdecision box 25 or box 125 to transfer control to Step 26 or Step 126.Either the precipitate of FIG. 1 or the solubilized liquid proteinsolution of FIG. 2 can be spray dried to form a pasteurized/sterilizedprotein powder, that can be used as a protein powder or added to foodsor drinks. Spray drying can be performed by commercially availableapparatus, such as a 30-inch Bowen Spray Drying unit, machine or a GEANiro Food Spray Dryer (Søborg, Denmark). Pre-treatment steps may betaken to prevent denaturing of the protein during the spray dryingprocess, and include, for example, adding sodium bicarbonate to thedewatered precipitate or solubilized liquid protein solution to a pHequal to or between about 6.5 to about 8.0.

The steps of the present invention include performing vacuum tumbling.Vacuum tumbling pulls water into the mixture uniformly. If vacuumtumbling is desired with the precipitate of FIG. 1 or the solubilizedliquid protein of FIG. 2, decision box 22A or box 122A transfers controlto Step 28 or Step 128. Vacuum tumbling may last for between about 20minutes to about 90 minutes. In the case of FIG. 1 using theprecipitate, Step 28, to add water to the protein precipitate mixture.In the case of FIG. 2, the solubilized liquid protein is tumbled withpieces of meat or animal muscle tissue to form a marinated meat product(e.g., marinated chicken or beef). A vacuum tumbler, such as a BIROManufacturing Model VTS-500 Vacuum Tumbler. The vacuum tumbling processpulls water into the mixture in a uniform way. In an embodiment, Step 28or Step 128 tumbles the pasteurized/sterilized protein precipitatemixture or solubilized liquid protein solution. The vacuum tumbling stepis optional. The resulting protein is a protein marinade.

In step 132 of FIG. 2, the pasteurized/sterilized solubilized liquidprotein solution can be evaporated under low heat to reduce the water ormoisture content to obtain a more condensed the pasteurized/sterilizedsolubilized liquid protein solution.

The resulting pasteurized/sterilized protein (e.g., thepasteurized/sterilized solubilized liquid protein solution or thepasteurized/sterilized precipitated protein) has a number ofcharacteristics. In one aspect, it does not contain undesirable levelsof pathogenic bacteria or its toxic contents. In another aspect, productof this invention is capable of meeting the definition of “finelytextured meat” (e.g., fat content of less than 30%; a protein content of14% or greater, by weight) or “lean finely textured meat” (e.g., fatcontent of less than 10%, a protein content of 14% or greater, byweight) as presently defined by the U.S. government. In an embodiment,the protein product of the present invention has about 14% or greater(e.g., about 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25%) by weightprotein and less than about 30% (less than about 25%, 20%, 15%, 10%, 9%,8%, 7%, 6%, 5%, 4%, 3%, 2%, 1%, 0%) by weight fat. In yet anotheraspect, the protein composition of the present invention also hasfunctionality of raw meat as measured from a measurement selected from awater binding test, a meat emulsion test, a moisture retention test, acolor test/observation, and a combination thereof. In an aspect, theprotein product of the present invention has a color of 75 to 20 L*,about 32 to 4 a*, and about 23 to 3 b*.

Thus, the precipitate or solubilized liquid protein solution can be used“as is” or then can be applied to raw meat for sale to consumers withoutcooking. The methods of the present invention result in a proteinprecipitate or solubilized liquid protein solution that is a functionalmeat composition. A “functional” meat composition is one that acts likeraw, uncooked meat. Surprisingly, the present invention provides thebenefits of cooked food because the meat composition ispasteurized/sterilized meat but looks and acts like raw meat. Functionalmeat is defined as a meat composition that acts like raw meat withrespect to one or more of the following characteristics: water binding,meat emulsion, moisture retention and/or a color. The present inventionincludes meat compositions that meet or exceed one or more of thesefunctional meat characteristics.

Water binding ability refers to the ability of thepasteurized/sterilized protein of the present invention to retain and/oruptake moisture and can be tested using the procedure of Hand et. al. “ATechnique to Measure the Water Uptake Properties of Meat,” 77^(th)Annual Meeting of the American Society of Animal Science, Paper No. 202(1985). Briefly, water binding ability can be determined by adding addedwater to meat, shaking it, and centrifuging it. After centrifugation,the centrifuged meat is placed on a mesh wire screen and then weighed.Meat products that undergo the steps of the present invention have awater binding ability that is the same or greater, as compared to meatthat does not undergo the steps of the present invention. In anembodiment, meat products that undergo the steps of the invention have awater binding ability that is about 1% to about 125% greater (e.g.,between about 40% and about 60% greater), as compared to meat that doesnot undergo the steps of the invention. See Example 1 in which 60% and110% water binding occurred with meat that underwent the steps of theinvention, as compared to the control.

Meat emulsion, sometimes referred to as fat emulsion, refers generallyto the ability for the inventive pasteurized/sterilized protein to bindor adhere to itself (e.g., its ability to stick together) and/or to forma protein matrix (e.g., a viscous meat batter). In an instance, thephrase “meat emulsion” refers to the binding ability of protein, fat,water and optionally other types of ingredients normally added to such amix (e.g., butter, mayonnaise, seasonings, and the like). One candetermine if a meat emulsion is formed by observation. It can also bemeasured in terms of its capacity (e.g., the maximum amount of fat oroil stabilized by a given amount of protein) or stability (the amount offat or oil retained or separated after stressing with heat the formedemulsion/batter).

Moisture retention refers to amount/content of moisture retained in thepasteurized/sterilized protein at any given time. Moisture retention ina meat product can be determined by using moisture analyzers (e.g.,Ohaus MB Model 25) or by observation (e.g., observing the amount ofmoisture that drips or escapes the meat). Meat products that undergo thesteps of the present invention have moisture retention that is also thesame or greater, as compared to meat that does not undergo the steps ofthe present invention. In an aspect, meat products that undergo thesteps of the invention have moisture that is about the same or about 1%to about 5% greater (e.g., between about 2% and about 3% greater), ascompared to meat that does not undergo the steps of the invention.Moisture retention can be controlled in the dewatering step so that, ifdesired, moisture retention can be brought down to its original moisturecontent.

The pasteurized/sterilized protein product of the methods of the presentinvention (see FIG. 1 or FIG. 2) results in muscle tissue proteinproduct that has a red color, namely a color of about 75 to 20 L*, about32 to 4 a*, and about 23 to 3 b*. The process of the present inventionenables protein product to look and act like raw or functional meat.Color is measured using the CIE L*a*b* color system in with dimension Lfor lightness and a* and b* for the color-opponent dimensions, based onXYZ coordinates. The L*a*b* color space includes all perceivable colors.In practice, the color is mapped using a three-dimensional integer forcolor representation. The lightness, L*, represents the darkest blackand the brightest white, while the a* axis opponent colors red and greenwhile the b* axis represents yellow and blue. Color can be measuredusing a color meter or colorimeter (e.g., CR-10 Plus from Konica Minolta(Ramsey, N.J., USA). The steps of the present invention surprisinglyresult in a lean meat that is red in color. The red color of the proteincomposition, is defined, in one aspect about 75 to 20 L*(e.g., 75, 74,73, 72, 71, 70, 69, 68, 67, 66, 65, 64, 63, 62, 61, 60, 59, 58, 57, 56,55, 54, 53, 52, 51, 50, 49, 48, 47, 46, 45, 44, 43, 42, 41, 40, 39, 38,37, 36, 35, 34, 33, 32, 31, 30 29, 28, 27, 26, 25, 24, 23, 22, 21, and20), about 32 to 4 a*(e.g., 32, 31, 30, 29, 28, 27, 26, 25, 24, 23, 22,21, 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, and 4)and about 23 to 3 b* (e.g., 23, 22, 21, 20, 19, 18, 17, 16, 15, 14, 13,12, 11, 10, 9, 8, 7, 6, 5, 4, and 3).

Unexpectedly it was found that the moisture binding ability of theproduct using the heated (pasteurized) protein was greater than themoisture binding ability obtained with heated (unpasteurized) protein.Also unexpectedly the appearance of the pasteurized product of thisinvention had the physical appearance including its red color of rawuncooked poultry without the addition of the protein product.

The end product can be added to food since it is pasteurized/sterilized.In one aspect of this invention, the composition of the presentinvention can be added to food such as ground meat, fish, poultry andthe like. For example, a marinade made by the present invention can beused to marinate meat, such as chicken (see Example 2). After marinatingchicken with and without the marinades made from the present invention,the uncooked chicken breast with the marinade of the present inventionpossessed about the same amount of moisture as the control marinade. Thecontrol marinade had a phosphate/salt preservative. After cooking, cookyield of the control and the chicken having the marinade of the presentinvention each had a cook yield of above about 80% (about 85%, 90%, 95%,or 100%). Generally, a marinade without a preservative will have a cookyield under 80%. Accordingly, the present invention allows for cookyields that mimic those obtained with preservatives (e.g.,phosphate/salt), without having to use the preservative. In anembodiment, marinades made from the present invention and incorporatedinto other meats have cook yields that are about the same, as comparedto that with preservatives.

The animal muscle tissue which undergoes the steps of the presentinvention include, for example, meat and fish, including shell fish.Representative suitable fish include deboned flounder, sole, haddock,cod, sea bass, salmon, tuna, trout or the like. Representative suitableshell fish include shelled shrimp, crabmeat, crayfish, lobster,scallops, oysters, or shrimp in the shell or the like. Representativesuitable meats include ham, beef, lamb, pork, venison, veal, buffalo orthe like; poultry such as chicken, mechanically deboned poultry meat,turkey, duck, a game bird or goose or the like either in fillet form orin ground form such as hamburger. In addition, meat products that can bemade using the steps of the present invention include animal muscletissue such as a sausage composition, a hot dog composition or anemulsified product. Sausage and hot dog compositions include ground meator poultry, herbs such as sage, spices, sugar, pepper, salt and fillerssuch as dairy products as is well known in the art.

EXEMPLIFICATION Example 1

The following example provides a measure of moisture retention in rawmeat treated with pasteurized protein product in accordance with thisinvention. This example uses cold processed chicken to determine whetherincreasing the homogenate temperature to a pasteurizing temperaturewould reduce moisture retention of raw chicken treated with pasteurizedprotein product. It is assumed that obtaining protein from whole chickenor mechanically deboned chicken would have no significant impact on themoisture retention properties of the final chicken product. That is,tests of protein made from cold processed chicken, rather than debonedchicken, should be a good predictor of moisture retention for proteinobtained from deboned chicken. In this example, step 12 performed mixingby using 1 part of chopped fresh chicken to 5 parts of chilled water byweight. The temperature of the mixture could be in the range of 34°F.≤T≤40° F. (i.e., 1° C.≤T≤4° C.). The specific temperature in the rangeof 34° F.≤T≤40° F. (i.e., 3° C.≤T≤4° C.) was used for this example.

Homogenizing the mixture in accordance with step 14 was performed with aSunbeam hand chopper. The hand chopper was operated for about 45seconds. This created an approximate particle size of 150 μm.

In step 16 the homogenate pH was lowered to about 2.8 by adding a liquid25% citric acid solution. This produced a chicken protein solution. AnOakton pH 6 Acorn series meter calibrated at pH4 and pH7 with standardbuffer solutions measured the pH.

In step 18, 235 grams of the chicken protein solution were placed into250 ml Erlenmeyer flasks. The flasks were placed in a 170° F. (i.e., 77°C.) water bath. A Taylor thermometer standardized by ice water measuredthe temperature which reached 160° F. (i.e., 71° C.) in approximately 15minutes. Step 20 immediately chilled the emulsion to 38° F. (i.e., 3°C.) by placing the Erlenmeyer flasks into an ice bath in a refrigeratorto aid in chilling,

During step 22 the pH of the chilled homogenate was treated toprecipitate the protein. In one sample 4% w/w sodium chloride was addedto a sample and the sample was stirred to achieve a pH of 2.25. Inanother sample, precipitation was induced by adjusting the pH to 4.8using powdered sodium bicarbonate.

Step 24 de-watered the protein flocculent obtained in step 22 by meansof an approximately 1,000 mesh strainer until the precipitate returnedto its approximate original moisture content of between 68.75% and84.75% with a mean of 78.21%.

Moisture tests were performed on the chicken samples using an Ohaus MBModel 25 moisture analyzer set on “Automatic Determination” with adrying temperature of 130° C. for an approximately 5 gram sample size,

To test the water binding ability, the above-identified procedure ofHand et. al. was used. 25 grams of protein were placed into pre-weighed,250 ml Nalgene Centrifuge bottles. Then 50 grams of 2° C. distilledwater were added to each of the centrifuge bottles. The bottles wereconsistently and vigorously shaken by hand for 30 seconds and thencentrifuged at 2° C. using a DuPont Sorvall RC-5B refrigeratedcentrifuge at 3,000 rpm for 10 minutes. The centrifuge bottles were thenremoved and immediately inverted over an approximate 1000 mesh wirescreen for 1 minute. Transfer of any solids that may have fallen fromthe tube onto the screen were put back into the tube and the tube wasthen re-weighed.

Table 2 identifies the percentage of water held per solid gram:

TABLE 2 % Moisture/Gram Treatment Protein Product of Protein Raw ChickenBreast/Control/ Unheated Proteins 140.2^(a) no steps of the inventionperformed Citric Acid (Step 16)/ Heated Proteins 224.2^(b) SodiumBicarbonate (Step 22) (Step 18) Unheated Proteins 141.1^(a) (no Step 18)Citric Acid (Step 16)/ Heated Proteins 297.8^(c) 4% Salt (Step 22)

Specifically, this information represents data obtained from n=24-30samples with p≤0.05 indicating a degree of confidence greater than 95%.Table 2 demonstrates that the data for the water binding ability forunheated proteins solubilized with citric acid and precipitated withsodium bicarbonate was statistically equal to the raw chicken breastswith unheated proteins. The data for the water binding ability forheated proteins using sodium bicarbonate for precipitation wassignificantly different from the data for unheated proteins. The datafor the water binding ability for heated proteins precipitated with saltwas significantly different from the data of both the unheated proteinsand from the data for the heated proteins precipitated with sodiumbicarbonate.

It is concluded that heating the homogenate at low pH was notdetrimental to the moisture retention of the final product. When thechicken breast was processed using citric acid to solubilize the proteinand sodium bicarbonate to precipitate the protein after heating thehomogenate to a pasteurizing temperature, the moisture per gram ofprotein significantly increased. This demonstrates that processingproteins in accordance with this invention by heating provides anunexpected result of actually improving the moisture retentionfunctionality of the product. A greater increase in moisture wasobtained by precipitating the heated proteins with a 4% salt solution.

Example 2

Protein Production

The following example provides a measure of moisture retention in cookedchicken treated with pasteurized, spray dried, protein product inaccordance with this invention that has been hydrated prior to use.

In this example, step 12 was performed mixing by using 1 part choppedfresh turkey breast to 5 parts chilled water by weight. The temperatureof the chilled water was 37° F. Homogenizing the mixture in accordancewith step 14 was performed with a Waring Model WSB immersion blender onhigh speed for two minutes. The pH of the homogenate was lowered to pH3.7 in step 16 using granular citric acid. An Oakton pH 6 Acorn seriesmeter calibrated at pH 4.01 and pH 7.00 with standard buffer solutionsmeasured the pH.

In step 18 approximately four gallons per batch of acidified, turkeyprotein solutions were heated on a Commercial Cooking Appliance ModelKR-S2 hot plate with constant stirring, until a temperature of 161° F.was achieved. A Control Company Traceable, infra-red thermometer wasused to determine the temperature of the solution. The thermometer wasstandardized against ice.

In step 20 the heated solution was chilled to a temperature <40° F. in arefrigerator. In step 22 the pH was adjusted using sodium bicarbonate(6% solution) to precipitate the protein. In step 24 the precipitate wasfiltered through a China cap with 1 mm holes to assist in de-watering.

In a pretreatment step, the partially de-watered protein precipitate wasfurther adjusted using powdered sodium bicarbonate until a pH of 6.8 wasachieved. The cooled neutralized protein solutions were packed into 5gallon bladder bags and transported under refrigeration for drying.

Spray Drying

In step 26 Spray drying was performed at Summit Custom Spray Drying,Flemington, N.J. on the protein solutions on a 30-inch Bowen SprayDrying unit. The inlet temperatures were 365-370° F., and the outlettemperatures were 225° F. Spray drying took place over a two day periodwith Day 1 resulting in 0.52 lbs. packed powder and 0.43 lbs. chambermaterial, and Day 2 resulting in 0.0775 lbs. packed powder and 0.28 lbs.chamber material. The packed protein powder was placed into polyethylenebags and analyzed for full nutritional and amino acid analysis.

Functionality

To test the moisture retention ability of the spray dried pasteurizedproteins a marinade was made using the proteins (re-hydrated), salt andwater as components. A comparison was performed using a standardphosphate marinade as a control. The control marinade was manufacturedusing 6% salt, 2.8% Brifisol 512 (phosphate), and 91.2% cold water (<40°F.). The ingredients were placed into a stainless steel mixing bowl andhomogenized using a Sunbeam kitchen hand mixer for 8 min. Thepasteurized protein marinade was made using 4% spray dried pasteurizedprotein, 6% salt and 90% cold water (<40° F.) and homogenized asdescribed above. The final pH's of the marinades were pH 6.84 for thephosphate/salt sample and pH 6.50 for the protein/salt sample. Themarinades were separately placed into a Marinade Express vacuum tumblerand rotated on slow (only) speed for 20 minutes with fresh chickenbreasts. The ratio of chicken to marinade was the same for both thecontrol and protein marinades (82% chicken to 18% marinade). Themarinated chicken breasts were weighed after vacuum tumbling and thecontrol pick up was 12.77% and the protein sample pick up was 13.21%.

After the vacuum tumbling step, cooked moisture retention was evaluatedby placing marinated chicken breasts onto sheet pans and placing thepre-weighed, marinated chicken breasts into a Cadco UNOX convection ovenset at 350° F., with convection on, for 30 minutes. After the 30 minutecook the breasts were allowed to set at room temperature for 5 minutesand weighed. The results of the experiment are shown in Table 3.

TABLE 3 Cook Yields for Marinated Chicken Breasts Breast Wgt. BreastWgt. After Cook Marinade Before Cook (g) Cook (g) Yield (%) Control(Phosphate/Salt) 309.03 276.39 89.44 264.86 215.79 81.47 305.62 252.1582.50 Average 84.47 Test (Protein/Salt) 273.78 242.40 88.54 288.44245.03 84.95 285.58 246.03 86.15 Average 86.55

DISCUSSION

Acidified turkey protein that was heated to pasteurizing temperatures(USDA Handbook Appendix A) and spray dried was shown to have improvedwater retaining ability on cooked product when used as a marinade andcompared to an industry standard, phosphate and salt. Typical results inthe industry for marinades containing salt and water alone (nophosphate) have cook yields under 80%.

This invention therefore provides a product that meets the variousobjectives of this invention. Specifically, this invention provides aprocess by which a protein product obtained from animal muscle ormechanically deboned meat can be used “as is” or added to raw meatwithout any cooking requirement to meet or exceed bacterial/pathogenregulations or specifications. Moreover, the addition of a proteinproduct obtained from mechanically deboned meat in accordance with thisinvention enhances functionality of the cooked food by increasing themoisture retention in the cooked food.

Example 3

Purpose:

Samples of beef were run through three differentsolubilization/precipitation procedures to determine if the finalproducts were similar or different in their characteristics, mainlycolor, to beef

Procedures:

Fresh beef (eye round roast (ERR); beef chuck, boneless pot shoulderroast (BPS)) was obtained for the testing. The protocols were asfollows:

Procedure 1: Citric—Solubilize in pH Less than 3.5:

200 g ground beef (ERR) was added to 1800 g (1:9) of cold water. Themixture was homogenized for 1.5 min using a Hamilton Beach hand mixer.The homogenate (pH 5.34) was made soluble using crystalline citric aciduntil a pH of 3.45 (as close to 3.5 as possible) was obtained. Theacidified homogenate was placed into a steel pot and heated slowly on ahotplate until a temperature of 138° F. was achieved and the temperatureheld for 19 minutes using constant stirring with a Teflon spatula.Temperature was monitored using an infrared thermometer. After the 19min hold time was met, the product was placed into a −20° F. freezer torapidly lower the temperature. The product was held in refrigeratedtemperatures at which time 1M sodium hydroxide was added until theproteins precipitated out of solution (pH 5.48). Product was centrifugedin a Sorvall RC-5B centrifuge for 10 min at 3,000 RPM. Collectedsediment product was then placed into glass petri dishes, with a lightedbackground and photographed and tested for color values (L,a,b) using aNix Mini Color Sensor supported with a iPhone app.

Procedure 2: HCl—Solubilize in pH Less than 3.5:

200 g ground beef (ERR) was added to 1800 g (1:9) of cold water. Themixture was homogenized for 1.5 min using a Hamilton Beach hand mixer.The homogenate (pH 5.34) was made soluble using 1 M HCl acid (44.46 g)until a pH of 3.47 (as close to 3.5 as possible) was obtained. Theacidified homogenate was placed into a steel pot and heated slowly on ahotplate until a temperature of 138° F. was achieved and the temperatureheld for 19 minutes using constant stirring with a Teflon spatula.Temperature was monitored using an infrared thermometer. After the 19min hold time was met, the product was placed into a −20° F. freezer torapidly lower the temperature. The product was held in refrigeratedtemperatures at which time 1M sodium hydroxide was added until theproteins precipitated out of solution (pH 5.47). Product was centrifugedin a Sorvall RC-5B centrifuge for 10 min at 3,000 RPM. Collectedsediment product was then placed into glass petri dishes, with a lightedbackground and photographed and tested for color values (L,a,b) using aNix Mini Color Sensor supported with a iPhone app.

Inventive Procedure 3: Acid to Base—Solubilize in pH from 3.6-4.2

400 g ground beef (ERR) was added to 800 g of cold water. The mixturewas homogenized for 1 min using a Hamilton Beach hand mixer. Thehomogenate was made soluble using crystalline citric acid (9.46 g) untila pH of 3.64 (as close to 3.6 as possible) was obtained. The acidifiedhomogenate was placed into a steel pot and heated slowly on a hotplateuntil a temperature of 138° F. was achieved and the temperature held for19 minutes using constant stirring with a Teflon spatula. Temperaturewas monitored using an infrared thermometer. After the 19 min hold timewas met, the product was placed into a −20° F. freezer to rapidly lowerthe temperature. Crystalline sodium carbonate was added until theproteins precipitated out of solution (pH 5.97). The suspension wasfiltered through a fine mesh stainless steel filter. Retentate productwas then placed into glass petri dishes, with a lighted background andphotographed and tested for color values (L,a,b) using a Nix Mini ColorSensor supported with a iPhone app.

Inventive Procedure 4: Base to Acid:

400 g ground beef (BPS) was added to 800 g of cold water. The mixturewas homogenized for 1 min using a Hamilton Beach hand mixer. Thehomogenate was made soluble using crystalline sodium carbonate (57.92 g)until a pH of 8.83 was obtained. The acidified homogenate was placedinto a steel pot and heated slowly on a hotplate until a temperature of138° F. was achieved and the temperature held for 19 minutes usingconstant stirring with a Teflon spatula. Temperature was monitored usingan infrared thermometer. After the 19 min hold time was met, the productwas placed into a −20° F. freezer to rapidly lower the temperature. Theproduct was held in refrigerated temperatures overnight at which timecrystalline citric acid was added until the proteins precipitated out ofsolution. The suspension was filtered through a fine mesh stainlesssteel filter. Product was then placed into glass petri dishes, with alighted background and photographed and tested for color values (L,a,b)using a Nix Mini Color Sensor supported with a iPhone app.

Results:

Procedures 1 and 2 (both below pH 3.5) resulted in a brown product andinventive Procedures 3 (pH of 3.6 or above) and 4 resulted in a redproduct. Color value results from both all four procedures are shownbelow:

Color Values (L, a, b) for the final products from the four Procedures(and Initial Beef) Product L a b Initial Ground Beef 34.2 24.7 16.4 34.525.1 16.5 34.8 25.3 16.9 35.0 25.5 16.2 34.9 24.5 16.4 Average 34.7 25.016.5 Product (Before Pasteurization) following the Procedure 2 -HCl, pH3.47 29.6 2.5 13.4 28.5 2.7 11.6 28.8 2.9 13.3 29.1 3.0 12.8 29.7 2.313.5 Average 29.1 2.7 12.9 Product (Before Pasteurization) following theProcedure 1-Citric, pH 3.45 30.6 2.2 11.2 31.3 2.4 12.1 33.1 2.7 12.230.3 2.7 11.5 31.7 2.7 12.2 Average 31.4 2.5 11.8 Product (BeforePasteurization) following the inventive Procedure 3-Acid to Base, pH3.64 23.8 5.2 9.1 23.3 5.0 8.8 24.6 4.3 10.2 24.0 5.6 10.4 24.4 4.4 10.1Average 24.0 4.9 9.7 Product (Before Pasteurization) following theinventive Procedure 4-(Base to Acid) 38.8 27.3 17.4 33.1 16.8 11.2 35.123.3 14.2 34.7 21.5 13.9 33.5 22.1 15.2 Average 35.0 22.2 14.4Precipitated product following the Procedure 2-HCl; pH 5.47 37.1 1.5 4.435.1 −0.2 2.8 34.3 −0.2 2.6 35.0 0.0 2.8 34.5 −0.3 2.5 Average 35.2 0.23.0 Precipitated product following the Procedure 1-Citric; pH 5.48 42.22.9 6.2 42.5 2.7 5.6 41.3 2.7 5.3 42.5 2.8 6.3 43.3 2.8 5.6 Average 42.42.8 5.8 Precipitated Inventive Procedure 3-(Acid to Base); pH 5.97 38.14.1 4.6 37.5 4.9 4.9 37.8 3.8 4.2 36.9 5.4 2.8 38.5 5.3 6.1 Average 37.84.7 4.5 Precipitated Inventive Procedure 4-(Base to Acid) 35.8 23.4 17.840.1 29.9 24.1 39.5 29.8 24.5 37.8 28.3 22.8 38.7 27.0 21.1 Average 38.427.7 22.1

DISCUSSION

One of the characteristics the present invention is that the finalproduct has the appearance of raw beef. One main attribute of raw beefis its red color. USDA requires that to use beef substitutes in anyfashion it has to have the color of beef in the raw form. L,a,b arethree values that establish a color's numerical point in a threedimensional space. Of the color values (L,a,b) the value most associatedwith red color is the “a” value. A very low or negative value points toa green color, whereas a high value trends toward a red color.

Surprisingly, it was found that, based on observation and empiricaldata, there was a clear delineation at pH 3.5 for protein productssolubilized with acid, pasteurized and precipitated with base.Solubilizing with an acid a pH of 3.5 or below resulted in a browncolored product, whereas solubilizing with an acid at a pH of 3.6 orabove resulted in a red, purple raw looking function protein. Inparticular, the product made using Procedures 1 or 2 using a pH of 3.5or less would not be considered raw beef due to its brown coloration,and therefore not accepted by USDA. Products made using the inventiveprocedure 3 or 4, have a higher “a value” and therefore have a redcolor, as compared to those seen in procedures 1 or 2. Further, the“a-value” of the Procedure 4 (Base to Acid) process is not only veryclose to the original starting raw beef, but surprisingly exceeds the“a-value.” In other words, the product of Procedure 4 resulted in aproduct that was even “more red” than raw beef without adding anycoloring.

Example 4

Experiment to Determine Color of Final Pasteurized, Non-PrecipitatedBeef Product

Purpose:

Samples of beef were run through two different solubilization,pasteurization procedures to determine if the final products weresimilar or different in their characteristics, mainly color, to beef

Procedures:

Fresh beef 93% lean ground beef chuck was obtained for the testing. Theprotocols were as follows:

Procedure 1-HCl: (Solubilize in pH Less than 3.5:)

200 g ground beef was added to 1800 g (1:9) of cold water. The mixturewas homogenized for 1.5 min using a Hamilton Beach hand mixer. Thehomogenate (pH 5.63) was made soluble using 1 M HCl acid (33.21 g) untila pH of 3.48 (as close to 3.5 as possible) was obtained. The acidifiedhomogenate was placed into a steel pot and heated slowly on a hotplateuntil a temperature of 138° F. was achieved and the temperature held for19 minutes using constant stirring with a Teflon spatula. Temperaturewas monitored using an infrared thermometer. After the 19 min hold timewas met, the product was placed into a −20° F. freezer to rapidly lowerthe temperature. Collected product was then placed into glass petridishes, with a lighted background and photographed and tested for colorvalues (L,a,b) using a Nix Mini Color Sensor supported with a iPhoneapp.

Inventive Procedure 2—Acid to Base (Solubilize in pH from 3.6-4.2):

400 g ground beef was added to 1200 g (1:3) of cold water. The mixturewas homogenized for 1.5 min using a Hamilton Beach hand mixer. Thehomogenate was made soluble using crystalline citric acid (7.39 g) untila pH of 3.63 (as close to 3.6 as possible) was obtained. The acidifiedhomogenate was placed into a steel pot and heated slowly on a hotplateuntil a temperature of 138° F. was achieved and the temperature held for19 minutes using constant stirring with a Teflon spatula. Temperaturewas monitored using an infrared thermometer. After the 19 min hold timewas met, the product was placed into a −20° F. freezer to rapidly lowerthe temperature. Product was then placed into glass petri dishes, with alighted background and photographed and tested for color values (L,a,b)using a Nix Mini Color Sensor supported with a iPhone app.

Inventive Procedure 3—Base to Acid:

400 g ground beef was added to 1200 g (1:3) of cold water. The mixturewas homogenized for 1.5 min using a Hamilton Beach hand mixer. Thehomogenate was made soluble using crystalline sodium carbonate (9.24 g)until a pH of 9.46 was obtained. The acidified homogenate was placedinto a steel pot and heated slowly on a hotplate until a temperature of138° F. was achieved and the temperature held for 19 minutes usingconstant stirring with a Teflon spatula. Temperature was monitored usingan infrared thermometer. After the 19 min hold time was met, the productwas placed into a −20° F. freezer to rapidly lower the temperature.Product was then placed into glass petri dishes, with a lightedbackground and photographed and tested for color values (L,a,b) using aNix Mini Color Sensor supported with a iPhone app.

Results:

Procedure 1 (below pH 3.5) resulted in a brown product and inventiveProcedures 2 (pH of 3.6 or above) and 3 resulted in a red product. Colorvalue results from both all three procedures are shown below:

Color Values (L, a, b) for the Products that were Pasteurized, with NoPrecipitation Product L a b Initial Ground Beef Homogenized (NoPasteurization) 39.7 17.0 13.4 39.3 15.7 12.9 39.8 18.7 14.4 37.7 13.211.9 38.6 14.9 12.8 Average 39.0 15.9 13.1 Procedure 1-HCl: pH 3.47;Pasteurized No Precipitation 25.6 2.4 5.5 25.9 2.3 5.4 24.4 3.0 6.2 25.52.7 5.8 25.0 2.7 5.9 Average 25.3 2.6 5.8 Inventive Procedure 3- Base toAcid: pH 9.46; Pasteurized No Precipitation 23.3 9.6 8.0 23.8 10.2 8.726.6 15.7 12.7 23.7 12.7 8.7 23.7 10.2 8.1 Average 24.2 11.7 9.2Inventive Procedure 2 - Acid to Base: pH 3.63; Pasteurized NoPrecipitation 30.3 4.2 5.2 29.6 3.6 4.7 30.2 4.1 4.8 30.7 4.5 5.4 29.94.5 5.0 Average 30.1 4.2 5.0

DISCUSSION

Of the color values (L,a,b) the value most associated with red color isthe “a value.” A very low or negative value points to a green color,whereas a high value trends toward a red color.

Surprisingly, it was found that, based on observation and empiricaldata, there was a clear delineation at pH 3.5 for protein productssolubilized with acid and pasteurized. Solubilizing with an acid a pH of3.5 or below resulted in a brown colored product, whereas solubilizingwith an acid at a pH of 3.6 or above resulted in a red, raw lookingfunction protein. In particular, the product made using Procedures 1using a pH of 3.5 or less would not be considered raw beef due to itsbrown coloration, and therefore not accepted by USDA. Products madeusing the inventive procedure 2 or 3, have a higher “a value” andtherefore have a red color, as compared to those seen in procedure 1.Further, the “a-value” of the Procedure 4 (Base to Acid) process issurprisingly very close to the original starting raw beef.

The terms about, approximately, substantially, and their equivalents maybe understood to include their ordinary or customary meaning. Inaddition, if not defined throughout the specification for the specificusage, these terms can be generally understood to represent values aboutbut not equal to a specified value. For example, “about” refers to 1% orless of a specified value e.g., 1%, 0.9%, 0.8%, 0.7%, 0.6%, 0.5%, 0.4%,0.3%, 0.2%, 0.1%, 0.09% of a specified value.

While this invention has been particularly shown and described withreferences to preferred embodiments thereof, it will be understood bythose skilled in the art that various changes in form and details may bemade therein without departing from the scope of the inventionencompassed by the appended claims.

The terms, comprise, include, and/or plural forms of each are open endedand include the listed items and can include additional items that arenot listed. The phrase “And/or” is open ended and includes one or moreof the listed items and combinations of the listed items.

The relevant teachings of all the references, patents and/or patentapplications cited herein are incorporated herein by reference in theirentirety.

What is claimed is: 1) A process for producing a protein product whereinthe protein product has a reduced pathogen level and retains afunctionality of raw meat, wherein the protein product is obtained fromanimal muscle tissue, the process comprises the steps of: A)homogenizing the animal muscle tissue, optionally in water, to therebyobtain a homogenate; B) adjusting the pH of the homogenate of step A) tosolubilize the protein to obtain a solubilized liquid protein solution;C) elevating the temperature of the solubilized liquid protein solutionof step B) to an internal temperature of 158° F. or above for at leastan instant, or to an internal temperature in a range between about 130°F. and about 157° F. for at least between about 14 seconds to about 121minutes such that the solubilized liquid protein solution ispasteurized, sterilized or both to obtain a solubilized liquid proteinsolution with a reduced pathogen level, wherein the reduced pathogenlevel comprises at least a reduction in salmonella by 6.5 log₁₀; and D)precipitating the protein from the solubilized liquid protein solutionof step C) to obtain a precipitated protein; wherein the precipitatedprotein has the reduced pathogen level as compared to a precipitatedprotein that has not undergone step C); and the precipitated proteinretains the functionality of raw meat. 2) The process of claim 1,wherein said pH adjustment for solubilizing the protein comprises theaddition of a food grade base to obtain a pH value in the range betweenabout 8.3 and about 10.5 or comprises the addition of a food grade acidto obtain a pH value in the range between about 3.6 and about 4.2. 3)The process of claim 1, wherein precipitating the protein from thesolubilized liquid protein solution includes the adding a food gradeacid to decrease the pH to a value in the range of 4.2≤pH≤6.4. 4) Theprocess of claim 1, further comprising vacuum tumbling the precipitatedprotein. 5) The process of claim 1, further comprising spray drying theprecipitated protein. 6) The process of claim 1, further comprisingadjusting the pH of the precipitated protein to a pH between about 6.5and about 8.0 and then spray drying the precipitated protein. 7) Theprocess of claim 1, further comprising chilling the solubilized liquidprotein solution with the reduced pathogen level of step C) to anintermediate temperature to obtain a chilled liquid protein solution. 8)The process of claim 1, wherein precipitating the protein from thesolubilized liquid protein solution of Step C) includes adding salt. 9)The process of claim 1, further comprising dewatering the precipitate toa desired moisture content. 10) The process of claim 1, assessing thefunctionality of the precipitated protein. 11) The process of claim 1,wherein the functionality of the precipitated protein of Step D) isdetermined from a measurement selected from the group consisting of:water binding test, meat emulsion test, moisture retention test, a colortest and a combination thereof. 12) The process of claim 1, wherein theprecipitated protein has a color in range between about 75 to 20 L*,about 32 to 4 a*, and about 23 to 3 b* 13) The process of claim 2,wherein the addition of the base in Step B) comprises adding a foodgrade base selected from the group consisting of: solution sodiumbicarbonate, sodium carbonate, potassium bicarbonate, potassiumcarbonate, sodium hydroxide any combination thereof. 14) The process ofclaim 2, wherein precipitating the protein of Step D) comprises adding afood grade acid selected from the group consisting of: citric acid,phosphoric acid, ascorbic acid, hydrochloric acid and any combinationthereof. 15) A protein product having a reduced pathogen level and afunctionality of raw meat, wherein the protein product is obtained fromanimal muscle tissue, the protein product is obtained by a processcomprising the steps of: A) homogenizing the animal muscle tissue,optionally in water, to thereby obtain a homogenate; B) adjusting the pHof the homogenate of step A) to solubilize the protein to obtain asolubilized liquid protein solution; C) elevating the temperature of thesolubilized liquid protein solution of step B) to an internaltemperature of 158° F. or above for at least an instant, or to aninternal temperature in a range between about 130° F. and about 157° F.for at least between about 14 seconds to about 121 minutes such that thesolubilized liquid protein solution is pasteurized, sterilized or bothto obtain a solubilized liquid protein solution with a reduced pathogenlevel, wherein the reduced pathogen level comprises at least a reductionin salmonella by 6.5 log₁₀; and D) precipitating the protein from thesolubilized liquid protein solution of step C) to obtain a precipitatedprotein; wherein the precipitated protein has the reduced pathogen levelas compared to a precipitated protein that has not undergone step C) andthe precipitated protein retains the functionality of raw meat. 16) Theprotein product of claim 15, the protein product is obtained by aprocess wherein said pH adjustment for solubilizing the proteincomprises the addition of a food grade base to obtain a pH value in therange between about 8.3 and about 10.5 or comprises the addition of afood grade acid to obtain a pH value in the range between about 3.6 andabout 4.2. 17) protein product of claim 15, the protein product isobtained by a process wherein precipitating the protein from thesolubilized liquid protein solution includes the adding a food gradeacid to decrease the pH to a value in the range of 4.2≤pH≤6.4. 18) Theprotein product of claim 15, the protein product is obtained by aprocess further comprising vacuum tumbling the precipitated protein. 19)The protein product of claim 15, the protein product is obtained by aprocess further comprising spray drying the precipitated protein. 20)The protein product of claim 15, the protein product is obtained by aprocess further comprising adjusting the pH of the precipitated proteinto a pH between about 6.5 and about 8.0 and then spray drying theprecipitated protein. 21) The protein product of claim 15, the proteinproduct is obtained by a process further comprising chilling thesolubilized liquid protein solution with the reduced pathogen level ofstep C) to an intermediate temperature to obtain a chilled liquidprotein solution. 22) The protein product of claim 15, the proteinproduct is obtained by a process wherein precipitating the protein fromthe solubilized liquid protein solution of Step C) includes adding salt.23) The protein product of claim 15, the protein product is obtained bya process further comprising dewatering the precipitate to a desiredmoisture content. 24) The protein product of claim 15, the proteinproduct is obtained by a process assessing the functionality of theprecipitated protein. 25) The protein product of claim 15, the proteinproduct is obtained by a process wherein the functionality of theprecipitated protein of Step D) is determined from a measurementselected from the group consisting of: water binding test, meat emulsiontest, moisture retention test, a color test and a combination thereof.26) The protein product of claim 15, the protein product is obtained bya process wherein the precipitated protein has a color in range betweenabout 75 to 20 L*, about 32 to 4 a*, and about 23 to 3 b* 27) Theprotein product of claim 16, the protein product is obtained by aprocess wherein the addition of the base in Step B) comprises adding afood grade base selected from the group consisting of: solution sodiumbicarbonate, sodium carbonate, potassium bicarbonate, potassiumcarbonate, sodium hydroxide any combination thereof. 28) The proteinproduct of claim 16, w the protein product is obtained by a processwherein precipitating the protein of Step D) comprises adding a foodgrade acid selected from the group consisting of: citric acid,phosphoric acid, ascorbic acid, hydrochloric acid and any combinationthereof. 29) A process for producing a protein product wherein theprotein product has a reduced pathogen level, and retains afunctionality of raw meat, wherein the protein product is obtained fromanimal muscle tissue, the process comprises the steps of: A)homogenizing the animal muscle tissue, optionally in water, to therebyobtain a homogenate; B) adjusting the pH of the homogenate of step A) tosolubilize the protein to obtain a solubilized liquid protein solution;C) elevating the temperature of the solubilized liquid protein solutionof step B) to an internal temperature of 158° F. or above for at leastan instant, or to an internal temperature in a range between about 130°F. and about 157° F. for at least between about 14 seconds to about 121minutes such that the solubilized liquid protein solution ispasteurized, sterilized or both to obtain a solubilized liquid proteinsolution with a reduced pathogen level, wherein the reduced pathogenlevel comprises at least a reduction in salmonella by 6.5 log₁₀; and D)adding the solubilized liquid protein solution with the reduced pathogenlevel of step C) to an animal muscle tissue to a protein product,wherein the solubilized liquid protein has the reduced pathogen level ascompared to a solubilized liquid protein that has not undergone step C)and the solubilized liquid protein retains the functionality of raw meat30) The process of claim 29, wherein adding the solubilized liquidprotein solution with the reduced pathogen level of step C) to theanimal muscle tissue comprises injecting the solubilized liquid proteinsolution with the reduced pathogen level of step C) into the animalmuscle tissue. 31) The process of claim 29, wherein adding thesolubilized liquid protein solution with the reduced pathogen level ofstep C) to an animal muscle tissue comprises spraying or applying thesolubilized liquid protein solution with the reduced pathogen level ofstep C) onto one or more surfaces of the animal muscle tissue. 32) Theprocess of claim 29, wherein the process further comprises chilling thesolubilized liquid protein solution with the reduced pathogen level ofstep C) to an intermediate temperature to obtain a chilled liquidprotein solution. 33) The process of claim 29, wherein said pHadjustment for solubilizing the protein comprises the addition of a foodgrade base to obtain a pH value in the range between about 8.3 and about10.5 or comprises the addition of a food grade acid to obtain a pH valuein the range between about 3.6 and about 4.2. 34) The process of claim29, wherein the precipitated protein has a color in range between about75 to 20 L*, about 32 to 4 a*, and about 23 to 3 b* 35) The process ofclaim 29, further comprising dewatering the solubilized liquid proteinto a desired moisture content. 36) The process of claim 29, furthercomprising spray-drying the solubilized liquid protein. 37) A proteinproduct having a reduced pathogen level and a functionality of raw meat,wherein the protein product is obtained from animal muscle tissue, theprotein product is obtained by a process comprising the steps of: A)homogenizing the animal muscle tissue, optionally in water, to therebyobtain a homogenate; B) adjusting the pH of the homogenate of step A) tosolubilize the protein to obtain a solubilized liquid protein solution;C) elevating the temperature of the solubilized liquid protein solutionof step B) to an internal temperature of 158° F. or above for at leastan instant, or to an internal temperature in a range between about 130°F. and about 157° F. for at least between about 14 seconds to about 121minutes such that the solubilized liquid protein solution ispasteurized, sterilized or both to obtain a solubilized liquid proteinsolution with a reduced pathogen level, wherein the reduced pathogenlevel comprises at least a reduction in salmonella by 6.5 log₁₀; and D)adding the solubilized liquid protein solution with the reduced pathogenlevel of step C) to an animal muscle tissue to a protein product,wherein the solubilized liquid protein has the reduced pathogen level ascompared to a solubilized liquid protein that has not undergone step C)and the solubilized liquid protein retains the functionality of rawmeat. 38) The protein product of claim 37, w the protein product isobtained by a process, wherein adding the solubilized liquid proteinsolution with the reduced pathogen level of step C) to the animal muscletissue comprises injecting the solubilized liquid protein solution withthe reduced pathogen level of step C) into the animal muscle tissue. 39)The protein product of claim 37, w the protein product is obtained by aprocess, wherein adding the solubilized liquid protein solution with thereduced pathogen level of step C) to an animal muscle tissue comprisesspraying or applying the solubilized liquid protein solution with thereduced pathogen level of step C) onto one or more surfaces of theanimal muscle tissue. 40) The protein product of claim 37, w the proteinproduct is obtained by a process, wherein the process further compriseschilling the solubilized liquid protein solution with the reducedpathogen level of step C) to an intermediate temperature to obtain achilled liquid protein solution. 41) The protein product of claim 37, wthe protein product is obtained by a process, wherein said pH adjustmentfor solubilizing the protein comprises the addition of a food grade baseto obtain a pH value in the range between about 8.3 and about 10.5 orcomprises the addition of a food grade acid to obtain a pH value in therange between about 3.6 and about 4.2. 42) The protein product of claim37, w the protein product is obtained by a process, herein theprecipitated protein has a color in range between about 75 to 20 L*,about 32 to 4 a*, and about 23 to 3 b* 43) The protein product of claim37, w the protein product is obtained by a process, further comprisingdewatering the solubilized liquid protein to a desired moisture content.